1H NMR evidence that almond "peptide: N-glycosidase" is an amidase. Kinetic data and trapping of the intermediate.

@article{Risley19851HNE,
  title={1H NMR evidence that almond "peptide: N-glycosidase" is an amidase. Kinetic data and trapping of the intermediate.},
  author={John M. Risley and Robert L Van Etten},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 29},
  pages={15488-94}
}
The enzyme from almond that catalyzes the hydrolysis of the N-glycosidic linkage between asparagine and the oligosaccharide chain of glycopeptides and glycoproteins has been variously termed an N-glycosidase and an amidase enzyme. Using turkey ovomucoid glycopeptide as a substrate for the enzyme, we followed the hydrolysis reaction by 1H NMR spectroscopy. These kinetic data revealed a rapid hydrolysis of the substrate but a delayed appearance of the final product. This implied that an… CONTINUE READING